Intermediates in the catalytic action of lipoyl dehydrogenase (diaphorase).
نویسندگان
چکیده
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منابع مشابه
The reversible conversion of lipoyl dehydrogenase to an artifactual enzyme by oxidation of sulfhydryl groups.
The effect of cupric ions on the activity, fluorescence, and absorbance, and on the sulfhydryl and flavin adenine dinucleotide contents, of lipoyl dehydrogenase has been examined. The changes take place in two phases during the reaction of the enzyme with copper ions. In the first phase, the lipoic activity of the enzyme decreases to about 10% of its initial value, while its diaphorase activity...
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The core-forming lipoate acetyltransferase (E2p) subunits of the pyruvate dehydrogenase (PDH) complex of Escherichia coli contain three tandemly repeated lipoyl domains although one lipoyl domain is apparently sufficient for full catalytic activity in vitro. Plasmids containing IPTG-inducible aceEF-IpdA operons which express multilip-PDH complexes bearing one N-terminal lipoyl domain and up to ...
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The inner lipoyl domain (L2) of the dihydrolipoyl acetyltransferase (E2) 60-mer forms a Ca(2+)-dependent complex with the pyruvate dehydrogenase phosphatase 1 (PDP1) or its catalytic subunit, PDP1c, in facilitating large enhancements of the activities of PDP1 (10-fold) or PDP1c (6-fold). L2 binding to PDP1 or PDP1c requires the lipoyl-lysine prosthetic group and specificity residues that distin...
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Particulate preparations from mammalian heart which are able to transfer electrons in successive steps from reduced diphosphopyridine nucleotide (DPNH) to molecular oxygen or to intermediate components of the respiratory chain have been reported from time to time (1, 2). Likewise, lipid-free, soluble DPNH dehydrogenases have been obtained from sarcosomal particles. Among them, the diaphorase of...
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3alpha-Hydroxysteroid dehydrogenase (3alpha-HSD) from Pseudomonas testosteronei and diaphorase (lipoyl dehydrogenase) from Clostridium spp were immobilized individually onto alkylamine glass beads through glutaraldehyde coupling. A cost-effective enzymic colorimetric method for determination of bile acid in the serum and bile was developed employing mixture of the immobilized enzymes. The metho...
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ورودعنوان ژورنال:
- The Biochemical journal
دوره 77 شماره
صفحات -
تاریخ انتشار 1960